title: Review. Structure and mechanism of ATP-binding cassette transporters.
abstract: ATP-binding cassette (ABC) transporters constitute a large superfamily of integral membrane proteins that includes both importers and exporters. In recent years, several structures of complete ABC transporters have been determined by X-ray crystallography. These structures suggest a mechanism by which binding and hydrolysis of ATP by the cytoplasmic, nucleotide-binding domains control the conformation of the transmembrane domains and therefore which side of the membrane the translocation pathway is exposed to. A basic, conserved two-state mechanism can explain active transport of both ABC importers and ABC exporters, but various questions remain unresolved. In this article, I will review some of the crystal structures and the mechanistic insight gained from them. Future challenges for a better understanding of the mechanism of ABC transporters will be outlined.
authors.affiliation: Institute of Molecular Biology and Biophysics, ETH Zurich, Zurich, Switzerland. locher@mol.biol.ethz.ch
authors.forename: Kaspar P
authors.initials: KP
authors.lastname: Locher
mesh_terms: D018528:ATP-Binding Cassette Transporters / Q000737:chemistry* / Q000145:classification / Q000378:metabolism*; D008958:Models, Molecular; D011487:Protein Conformation; D017434:Protein Structure, Tertiary
chemical_list: D018528:ATP-Binding Cassette Transporters